The objective of the overall research in this laboratory is centered on achieving as complete a description as possible for the structures of peptides, proteins, nucleic acids and their complexes in solution, principally by NMR spectroscopy. At present particular emphasis is being placed on developing approaches which allow the investigation of larger and complex systems as well as increase the precision with which these solution structures can be obtained. Experiments aimed at investigating protein folding are conducted and structural polymorphism is evaluated. Structural studies for several proteins have been carried out. These comprise HIV-1 protease, cyanovirin-N and a variety of variants thereof,ubiquitin and a replication initiator protein. In addition, work was also carried out on different quaternary states of the model protein GB1 and on folding intermediates. New experiments were devised for measuring residual dipolar couplings.